PTFAH_HAEIN
ID PTFAH_HAEIN Reviewed; 499 AA.
AC P44715;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Multiphosphoryl transfer protein {ECO:0000303|PubMed:8763608};
DE Short=MTP {ECO:0000303|PubMed:8763608};
DE AltName: Full=Diphosphoryl transfer protein {ECO:0000250|UniProtKB:P69811};
DE Short=DTP {ECO:0000250|UniProtKB:P69811};
DE AltName: Full=Phosphotransferase FPr protein {ECO:0000303|PubMed:8763608};
DE AltName: Full=Pseudo-HPr {ECO:0000303|PubMed:8763608};
DE Includes:
DE RecName: Full=Phosphocarrier protein HPr {ECO:0000303|PubMed:8763608};
DE Short=Protein H {ECO:0000303|PubMed:8763608};
DE Includes:
DE RecName: Full=PTS system fructose-specific EIIA component {ECO:0000303|PubMed:8763608};
DE AltName: Full=EIIA-Fru {ECO:0000303|PubMed:8763608};
DE AltName: Full=EIII-Fru {ECO:0000303|PubMed:8763608};
DE AltName: Full=Fructose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:8763608};
GN Name=fruB; OrderedLocusNames=HI_0448;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, AND DOMAIN STRUCTURE.
RX PubMed=8763608; DOI=10.1016/0923-2508(96)81381-7;
RA Reizer J., Reizer A., Saier M.H. Jr.;
RT "Novel PTS proteins revealed by bacterial genome sequencing: a unique
RT fructose-specific phosphoryl transfer protein with two HPr-like domains in
RT Haemophilus influenzae.";
RL Res. Microbiol. 147:209-215(1996).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II FruAB PTS system is involved in fructose transport.
CC {ECO:0000250|UniProtKB:P69811, ECO:0000305|PubMed:8763608}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by fructose and repressed by FruR.
CC {ECO:0000250|UniProtKB:P17127}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417,
CC ECO:0000269|PubMed:8763608}.
CC -!- DOMAIN: In contrast to classical PTS systems, the fructose-specific PTS
CC has no requirement for HPr; FruB combines a IIA domain with two HPr
CC domains. {ECO:0000269|PubMed:8763608}.
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DR EMBL; L42023; AAC22107.1; -; Genomic_DNA.
DR PIR; B64069; B64069.
DR RefSeq; NP_438609.1; NC_000907.1.
DR RefSeq; WP_005693713.1; NC_000907.1.
DR AlphaFoldDB; P44715; -.
DR SMR; P44715; -.
DR STRING; 71421.HI_0448; -.
DR DNASU; 950651; -.
DR EnsemblBacteria; AAC22107; AAC22107; HI_0448.
DR KEGG; hin:HI_0448; -.
DR PATRIC; fig|71421.8.peg.468; -.
DR eggNOG; COG1925; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_046384_0_0_6; -.
DR OMA; QGIEWGE; -.
DR PhylomeDB; P44715; -.
DR BioCyc; HINF71421:G1GJ1-464-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00367; PTS-HPr_like; 2.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 3.30.1340.10; -; 2.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016258; FruB.
DR InterPro; IPR000032; HPr-like.
DR InterPro; IPR035895; HPr-like_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR001020; PTS_HPr_His_P_site.
DR InterPro; IPR002114; PTS_HPr_Ser_P_site.
DR Pfam; PF00381; PTS-HPr; 2.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR PIRSF; PIRSF000690; Fruc_PTS_diPryltransf; 1.
DR PRINTS; PR00107; PHOSPHOCPHPR.
DR SUPFAM; SSF55594; SSF55594; 2.
DR SUPFAM; SSF55804; SSF55804; 2.
DR TIGRFAMs; TIGR01003; PTS_HPr_family; 2.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51350; PTS_HPR_DOM; 2.
DR PROSITE; PS00369; PTS_HPR_HIS; 2.
DR PROSITE; PS00589; PTS_HPR_SER; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Repeat; Sugar transport; Transferase; Transport.
FT CHAIN 1..499
FT /note="Multiphosphoryl transfer protein"
FT /id="PRO_0000186520"
FT DOMAIN 2..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT DOMAIN 286..376
FT /note="HPr 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:8763608"
FT DOMAIN 410..499
FT /note="HPr 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681,
FT ECO:0000305|PubMed:8763608"
FT REGION 155..285
FT /note="M domain"
FT /evidence="ECO:0000305|PubMed:8763608"
FT REGION 378..409
FT /note="Linker"
FT /evidence="ECO:0000305|PubMed:8763608"
FT ACT_SITE 62
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 300
FT /note="Pros-phosphohistidine intermediate; for HPr 1
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT ACT_SITE 424
FT /note="Pros-phosphohistidine intermediate; for HPr 2
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00681"
FT MOD_RES 62
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 300
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305"
FT MOD_RES 424
FT /note="Phosphohistidine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 53007 MW; D6DDC99884A58C63 CRC64;
MLELSESNIH LNANAIDKQQ AIEMAVSALV QAGNVENGYL QGMLARELQT STFLGNGIAI
PHGTLDTRLM VKKTGVQVFQ FPQGIEWGEG NIAYVVIGIA ARSDEHLSLL RQLTHVLSDE
DTAAKLAKIT DVAEFCAILM GETIDPFEIP AANISLDVNT QSLLTLVAIN AGQLQVQSAV
ENRFISEVIN NAALPLGKGL WVTDSVVGNV KNALAFSRAK TIFSHNGKAV KGVITVSAVG
DQINPTLVRL LDDDVQTTLL NGNSTEILTA LLGSSSDVET QSVEGAVVGT FTIRNEHGLH
ARPSANLVNE VKKFTSKITM QNLTRESEVV SAKSLMKIVA LGVTQGHRLR FVAEGEDAKQ
AIESLGKAIA NGLGENVSAV PPSEPDTIEI MGDQIHTPAV TEDDNLPANA IEAVFVIKNE
QGLHARPSAI LVNEVKKYNA SVAVQNLDRN SQLVSAKSLM KIVALGVVKG TRLRFVATGE
EAQQAIDGIG AVIESGLGE
